MRC1_SCHPO
ID MRC1_SCHPO Reviewed; 1019 AA.
AC Q9P7T4;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Mediator of replication checkpoint protein 1;
DE AltName: Full=DNA replication checkpoint mediator mrc1;
GN Name=mrc1; ORFNames=SPAC694.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, INTERACTION WITH CDS1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP SER-604 AND THR-645, AND MUTAGENESIS OF SER-599; SER-604; SER-614; THR-634;
RP SER-637 AND THR-645.
RX PubMed=14585996; DOI=10.1128/mcb.23.22.8395-8403.2003;
RA Zhao H., Tanaka K., Nogochi E., Nogochi C., Russell P.;
RT "Replication checkpoint protein Mrc1 is regulated by Rad3 and Tel1 in
RT fission yeast.";
RL Mol. Cell. Biol. 23:8395-8403(2003).
CC -!- FUNCTION: Component of the replisome and is required for rad3-dependent
CC activation of the checkpoint kinase cds1 in response to replication
CC fork arrest. Phosphorylation allows it to mediate the activation of
CC cds1. {ECO:0000269|PubMed:14585996}.
CC -!- SUBUNIT: Interacts with cds1. {ECO:0000269|PubMed:14585996}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14585996}.
CC Note=Associated with chromatin.
CC -!- PTM: Phosphorylated by rad3 and tel1. {ECO:0000269|PubMed:14585996}.
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DR EMBL; CU329670; CAB71844.1; -; Genomic_DNA.
DR PIR; T50251; T50251.
DR RefSeq; NP_594486.1; NM_001019915.2.
DR AlphaFoldDB; Q9P7T4; -.
DR SMR; Q9P7T4; -.
DR BioGRID; 279668; 124.
DR ELM; Q9P7T4; -.
DR IntAct; Q9P7T4; 1.
DR MINT; Q9P7T4; -.
DR STRING; 4896.SPAC694.06c.1; -.
DR iPTMnet; Q9P7T4; -.
DR MaxQB; Q9P7T4; -.
DR PaxDb; Q9P7T4; -.
DR PRIDE; Q9P7T4; -.
DR EnsemblFungi; SPAC694.06c.1; SPAC694.06c.1:pep; SPAC694.06c.
DR GeneID; 2543240; -.
DR KEGG; spo:SPAC694.06c; -.
DR PomBase; SPAC694.06c; mrc1.
DR VEuPathDB; FungiDB:SPAC694.06c; -.
DR eggNOG; ENOG502QSP5; Eukaryota.
DR HOGENOM; CLU_301308_0_0_1; -.
DR InParanoid; Q9P7T4; -.
DR OMA; YQIKDQK; -.
DR PhylomeDB; Q9P7T4; -.
DR Reactome; R-SPO-176187; Activation of ATR in response to replication stress.
DR PRO; PR:Q9P7T4; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0031298; C:replication fork protection complex; ISO:PomBase.
DR GO; GO:0070337; F:3'-flap-structured DNA binding; IDA:PomBase.
DR GO; GO:0010997; F:anaphase-promoting complex binding; IBA:GO_Central.
DR GO; GO:0000405; F:bubble DNA binding; IDA:PomBase.
DR GO; GO:0062037; F:D-loop DNA binding; IDA:PomBase.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:PomBase.
DR GO; GO:0035591; F:signaling adaptor activity; IGI:PomBase.
DR GO; GO:0000403; F:Y-form DNA binding; IDA:PomBase.
DR GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IMP:PomBase.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:PomBase.
DR GO; GO:1903466; P:regulation of mitotic DNA replication initiation; IMP:PomBase.
DR GO; GO:0011000; P:replication fork arrest at mating type locus; IMP:PomBase.
DR GO; GO:0031582; P:replication fork arrest at rDNA repeats; IMP:PomBase.
DR GO; GO:0090001; P:replication fork arrest at tRNA locus; IMP:PomBase.
DR GO; GO:0048478; P:replication fork protection; IPI:PomBase.
DR InterPro; IPR024146; Claspin.
DR InterPro; IPR018564; Repl_chkpnt_MRC1_dom.
DR PANTHER; PTHR14396; PTHR14396; 1.
DR Pfam; PF09444; MRC1; 1.
PE 1: Evidence at protein level;
KW DNA replication; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1019
FT /note="Mediator of replication checkpoint protein 1"
FT /id="PRO_0000096573"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14585996"
FT MOD_RES 645
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:14585996"
FT MUTAGEN 599
FT /note="S->A: Severe hydroxyurea (HU) sensitivity."
FT /evidence="ECO:0000269|PubMed:14585996"
FT MUTAGEN 604
FT /note="S->A: Severe hydroxyurea (HU) sensitivity."
FT /evidence="ECO:0000269|PubMed:14585996"
FT MUTAGEN 614
FT /note="S->A: Severe hydroxyurea (HU) sensitivity."
FT /evidence="ECO:0000269|PubMed:14585996"
FT MUTAGEN 634
FT /note="T->A: Hydroxyurea (HU) sensitivity."
FT /evidence="ECO:0000269|PubMed:14585996"
FT MUTAGEN 637
FT /note="S->A: Hydroxyurea (HU) sensitivity."
FT /evidence="ECO:0000269|PubMed:14585996"
FT MUTAGEN 645
FT /note="T->A: Hydroxyurea (HU) sensitivity."
FT /evidence="ECO:0000269|PubMed:14585996"
SQ SEQUENCE 1019 AA; 114319 MW; 6B5E7A4B5ABE5380 CRC64;
MASLDENADE LHRMDSSDEA SINDDQEDIL DTPRTRVRKM LASVDMQLSS NAVSEASLDK
ESTVGNLENQ KNRSYSSEIY LHSDTNFLSN FDSAYERVRR LLNQQGGKSS LQKKEVEQIE
TQEGGDNAKG SPSSENKDSD RNSRLQQLIE KKRNALKKEQ EDLIQNSATS HSKSDNLDSE
SADDSDLADE SELSKKYTSD RKIRNASKKA LLELHRNTAR LTRETALKPE VVVKKKVTLR
EFFQKIGFKN DNQLENKAIS EEEANSTEPP NVEKEEPKPS VDRSTGIVNS EDIKELSVED
DSLELKEITP EALDIGQTSL FTTLNQTQVK KEDNKKFLLK EINAKLNEDD IDSELEIEVK
PKTTALDNIE KSKLSEENEH GIKGKLKQLA EIKLSKDGKP FENEFNIKSF NRNLVKRAAV
MAKLQRNQLE EELKAKGIYK PTIQGEKEEE EDPLERARND AEKIRQLEKA SGNASDEGEL
NDEEEVISSS NTPSTKAKTT NKVIISDVII EATQAEPKRR QKNSRVVFDE EDLTGDSHGS
SNMKISESDD ESNGDMIRDS FDRLSSESIK DSQKTEELHD SFGINDEVDQ STSLYVQNSQ
PSASQLTIVD ATYSQPPPRW ESSSRDDKTN TSSTQPSQVD SLVPTQLDST IPTQIDSVQR
NKDQDDEEIL EERRESRRDS KTFLSRTMLY NKDTGKADSA WASDLIEEQA IESDDEYAGI
GGLSDDGLSD SDAELEVQNM IDDETTIQKG EVASMAQFAK DQEMDRDEKL VKQLMKDVTT
GALRKRNRNG FAALDDSDDE DYSNLRREKL KELRRQKLLE DGNLNVLEGD KRKAFLATVE
DSLVSSKDNL TWLDATVEDS GVGSSDLGDE YLYSEQSLNH EEEEQMEEEL SEIFSSGGPN
VVDRVYLKKS STRHTSDNNS LEEVLPIFPG VRKLVSNSQS EKIGDLSNDN SMGAKSYKTP
IISSTQRPQG RKFRGLMNQS SKADISRTVD AGSIKVVPNS QSANPPRLLA SLNNYSDFD
